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Database: UniProt
Entry: A0A0H2SDI9_9AGAM
LinkDB: A0A0H2SDI9_9AGAM
Original site: A0A0H2SDI9_9AGAM 
ID   A0A0H2SDI9_9AGAM        Unreviewed;      1262 AA.
AC   A0A0H2SDI9;
DT   16-SEP-2015, integrated into UniProtKB/TrEMBL.
DT   16-SEP-2015, sequence version 1.
DT   24-JAN-2024, entry version 27.
DE   RecName: Full=PhoX domain-containing protein {ECO:0008006|Google:ProtNLM};
GN   ORFNames=SCHPADRAFT_283259 {ECO:0000313|EMBL:KLO15031.1};
OS   Schizopora paradoxa.
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC   Hymenochaetales; Schizoporaceae; Schizopora.
OX   NCBI_TaxID=27342 {ECO:0000313|EMBL:KLO15031.1, ECO:0000313|Proteomes:UP000053477};
RN   [1] {ECO:0000313|EMBL:KLO15031.1, ECO:0000313|Proteomes:UP000053477}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=KUC8140 {ECO:0000313|EMBL:KLO15031.1,
RC   ECO:0000313|Proteomes:UP000053477};
RG   DOE Joint Genome Institute;
RA   Min B., Park H., Jang Y., Kim J.-J., Kim K.H., Pangilinan J., Lipzen A.,
RA   Riley R., Grigoriev I.V., Spatafora J.W., Choi I.-G.;
RT   "Complete genome sequence of Schizopora paradoxa KUC8140, a cosmopolitan
RT   wood degrader in East Asia.";
RL   Submitted (APR-2015) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the sorting nexin family.
CC       {ECO:0000256|ARBA:ARBA00010883}.
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DR   EMBL; KQ085935; KLO15031.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0H2SDI9; -.
DR   STRING; 27342.A0A0H2SDI9; -.
DR   InParanoid; A0A0H2SDI9; -.
DR   OrthoDB; 5392990at2759; -.
DR   Proteomes; UP000053477; Unassembled WGS sequence.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR   GO; GO:0035091; F:phosphatidylinositol binding; IEA:InterPro.
DR   GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR   Gene3D; 3.30.1520.10; Phox-like domain; 1.
DR   Gene3D; 1.10.167.10; Regulator of G-protein Signalling 4, domain 2; 1.
DR   InterPro; IPR003114; Phox_assoc.
DR   InterPro; IPR001683; PX_dom.
DR   InterPro; IPR036871; PX_dom_sf.
DR   InterPro; IPR016137; RGS.
DR   InterPro; IPR036305; RGS_sf.
DR   InterPro; IPR044926; RGS_subdomain_2.
DR   InterPro; IPR013937; Sorting_nexin_C.
DR   PANTHER; PTHR22775; SORTING NEXIN; 1.
DR   PANTHER; PTHR22775:SF3; SORTING NEXIN-13; 1.
DR   Pfam; PF08628; Nexin_C; 1.
DR   Pfam; PF00787; PX; 1.
DR   Pfam; PF02194; PXA; 1.
DR   Pfam; PF00615; RGS; 1.
DR   SMART; SM00312; PX; 1.
DR   SMART; SM00313; PXA; 1.
DR   SMART; SM00315; RGS; 1.
DR   SUPFAM; SSF64268; PX domain; 1.
DR   SUPFAM; SSF48097; Regulator of G-protein signaling, RGS; 1.
DR   PROSITE; PS50195; PX; 1.
DR   PROSITE; PS51207; PXA; 1.
DR   PROSITE; PS50132; RGS; 1.
PE   3: Inferred from homology;
KW   Coiled coil {ECO:0000256|SAM:Coils}; Membrane {ECO:0000256|SAM:Phobius};
KW   Reference proteome {ECO:0000313|Proteomes:UP000053477};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        6..26
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        33..58
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          109..301
FT                   /note="PXA"
FT                   /evidence="ECO:0000259|PROSITE:PS51207"
FT   DOMAIN          438..582
FT                   /note="RGS"
FT                   /evidence="ECO:0000259|PROSITE:PS50132"
FT   DOMAIN          885..1003
FT                   /note="PX"
FT                   /evidence="ECO:0000259|PROSITE:PS50195"
FT   REGION          658..680
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          738..766
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          547..575
FT                   /evidence="ECO:0000256|SAM:Coils"
SQ   SEQUENCE   1262 AA;  140003 MW;  F90EBACCC11252DD CRC64;
     MVEFGSQTAI GVGVLAILIP VCLRVLSPWT VVFFLFPTLL FLVGFACLFA TVIAGYFLDK
     YRPTKHRNEL SSIVRPLAFS TPAAWQAVQT RSRWSYKSPQ NLSPLRPDFP VASAAINDIL
     ILIVRDFVLT WYRDLSDSPS FPAAVSECLH DTLDDLLERL ANIDLSSFVV RRVFPKLTIH
     VDQFRHSETT LRGAGLERHL TQSEELDLLL ASRYVGKGGA LHPAVDNLSS TFTKQTEESH
     LRKLVDAALP VILPAKDAKS KALHIVVREI VACAVLAPIT EMLSDPDFWN RTIEQLAGAA
     IRQQKLISKV RSVLEIQSLS PAAQPSKDGR HQQHEVITMR TDPRHFEGFL RSISRCNSLL
     DARRLKNDIV GEIRRTRTLL ASHENEDWIN GHKTEDVVAF LDRLYTAKRK IEKRIVLLGG
     QDEAGSISSS DNARTNFSLR DVLGNPSSLS HFMEFMDRRG RSLLVQFWLT VESFKNPLES
     LDSDTDADED AAALQSGGKT LQEDLTMIND LYFSQSVVPQ ALSMISRKHV DAVRAYAGKP
     SASFSEERKA RRAVMRAQKQ VEQEMENEFE EFKRSDLWFR AVSDLEIRPV QEKIVQAPAL
     SSKPSQASSA TGILSSFVQG LTSDKHVAST NPRQIPRVAS ASAALPVVTK SNLSREFERP
     ELPYPAPGAG RSVSAQAPSH SMEVLMSPSA DSDSGSARAP LFDEAEDGTL LSADADEAQR
     MEAIHAAVTD IIASENRLSV DEGSGKKSRS EESLQNALFP PEDKKSVGGK GVSGYFDGAL
     DGIDEDNATE ANEVDEMMSS SFHPAGPGDL HLSNEISRLG EKIGHLQSQD VILDTLIRKA
     ELTGDAQELK LLRRSKSALV RELRQLVFQK SQYEQQDMAN KLIPGRTNAS IVNSTVGEED
     GKSVVRYLIE VQQLGPDGSF ASGWVVARRY SEFLFMHQHL RDQYLPVKNL DFPGKRLLSS
     SSAVATDSRR VGLEKYLQNL LIIPMVCESQ ELRTFLSRES PFMTQTPSTS TSSKDTPAFL
     GHNIVRSVVK SFTESIDDMF FGPSMLDVMI GRLTRQAAEF AGIVGTASTD EDLVTQALKA
     SGKSVPEETL IQLPGDLKPL EGETSSSSFT APICDFILSL FELDKKNNWL RRQAIVIILQ
     QVLGDTIERK FRDTVKAYLD ESHLMTYINI FKDGLWPGGK LKASGPPRTV EEKARTRDEA
     NRKLSTLLPD VAANMMGRSN ARRGARRMFA VLQNRRLNQH IVYTILDEVF IALFPELPKP
     TS
//
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